Earticle

초록

영어

Collectins are a family of collagenous calcium-dependent defense lectins in animals. Their polypeptide chains consist of four regions: a cysteine-rich N-terminal domain, a collagen-like region, an alpha-helical coiled-coil neck domain and a C-terminal lectin or carbohydrate-recognition domain. These polypeptide chains form trimers that may assemble into larger oligomers. The best studied family members are the mannan-binding lectin, which is secreted into the blood by the liver, and the surfactant proteins A and D, which are secreted into the pulmonary alveolar and airway lining fluid. The collectins represent an important group of pattern recognition molecules, which bind to oligosaccharide structures and/or lipid moities on the surface of microorganisms. Collectin placenta 1 (CL-P1), a recently discovered scavenger receptor, mediates the uptake of oxidized low density lipoprotein and microbes. In this study, we investigated CL-P1-mediated binding and ingestion of yeast-derived zymosan bioparticles using Chinese hamster ovary (CHO) cells stably expressing human CL-P1 (CHO/CL-P1) and human vascular endothelial cells constitutively expressed CL-P1. The uptake of zymosan by CHO/CL-P1 was dependent upon the level of CL-P1 expressed on the membrane and was inhibited by cytochalasin D and wortmannin. The binding of zymosan was also inhibited by ligands of other scavenger receptors such as poly(I) and dextran sulfate. Real time reverse transcription-PCR analyses showed that other scavenger receptors, namely LOX-1, Stabilin-2, or macrophage receptor with collagenous structure (MARCO), were not expressed in human umbilical vein endothelial cells isolated from different individuals. Nonopsonic zymosan ingestion was inhibited in three primary cultured vascular endothelial cells, including different human umbilical vein endothelial cells from nine individuals treated with CL-P1 small interfering RNAs (siRNAs), although small interfering RNAs of other scavenger receptors had no effect on zymosan uptake in these cells. Furthermore, we confirmed that CL-P1 is expressed in human and murine vascular endothelial layers. Our results demonstrated that CL-P1 predominantly mediated phagocytosis for fungi in vascular endothelia.

저자

• SeongJae Jang [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]
• Atsushi Fukuoh [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]
• Katsuki Ohtani [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]
• Kenichiro Mori [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]
• Itsuro Yoshida [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]
• Yasuhiko Suzuki [ Department of Global Epidemiology, Hokkaido University Research Center for Zoonosis Control, Sapporo, 060-0818, Japan ]
• Nobutaka Wakamiya [ Department of Microbiology and Immunochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614